O-succinylbenzoate—CoA ligase: Difference between revisions
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{{Infobox enzyme |
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{{Enzyme |
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| Name = |
| Name = ''o''-Succinylbenzoate—CoA ligase |
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| EC_number = 6.2.1.26 |
| EC_number = 6.2.1.26 |
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| CAS_number = 72506-70-8 |
| CAS_number = 72506-70-8 |
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| IUBMB_EC_number = 6/2/1/26 |
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'''''o''-Succinylbenzoate—CoA ligase''' ({{EnzExplorer|6.2.1.26}}), encoded from the menE gene in ''Escherichia coli'', catalyzes the fifth reaction in the synthesis of [[menaquinone]] (vitamin K2). This pathway is called 1, 4-dihydroxy-2-naphthoate biosynthesis I.<ref>{{Cite book|title = Phylloquinone (Vitamin K1): function, enzymes and genes|last = van Oostende, Widhalm, Furt, Ducluzeau, Basset|publisher = Academic Press (Amsterdam)|year = 2011|location = Advances in Botanical Research|pages = 229–61}}</ref> [[Vitamin K]] is a [[quinone]] that serves as an electron transporter during [[anaerobic respiration]]. This process of anaerobic respiration allows the bacteria to generate the energy required to survive. |
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== Background == |
== Background == |
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The systematic name for the MenE enzyme is ''2-succinylbenzoate: CoA ligase (AMP-forming)''. Other names for this enzyme include: o-succinylbenzoate-CoA synthase; o-succinylbenzoyl-coenzyme A synthetase; OSB-CoA synthetase; OSB: CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. The EC number is 6.2.1.26. MenE belongs to the ligase enzyme family, or class 6. |
The [[List of enzymes|systematic name]] for the MenE enzyme is ''2-succinylbenzoate: CoA ligase (AMP-forming)''. Other names for this enzyme include: o-succinylbenzoate-CoA synthase; o-succinylbenzoyl-coenzyme A synthetase; OSB-CoA synthetase; OSB: CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. The EC number is 6.2.1.26. MenE belongs to the ligase enzyme family, or class 6. |
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In the presence of 0.5mM of Ca(2+), K(+), Na(+), and Zn(2+) the enzyme activity was increased twofold. In the presence of .5 mM of Co(2+) and Mn(2+) the enzyme activity was increased fourfold. Mg(2+) is the ion that increases the enzyme activity the most. With .5 mM of Mg(2+) enzyme activity was increased sixfold. Inhibitors of this enzyme include [[diethylprocarbonate]], Fe(2+), Hg(2+), and Mg(2+) (above 1mM).<ref>{{ |
In the presence of 0.5mM of Ca(2+), K(+), Na(+), and Zn(2+) the enzyme activity was increased twofold. In the presence of .5 mM of Co(2+) and Mn(2+) the enzyme activity was increased fourfold. Mg(2+) is the ion that increases the enzyme activity the most. With .5 mM of Mg(2+) enzyme activity was increased sixfold. Inhibitors of this enzyme include [[diethylprocarbonate]], Fe(2+), Hg(2+), and Mg(2+) (above 1mM).<ref name = "Kwon_1996">{{cite journal | vauthors = Kwon O, Bhattacharyya DK, Meganathan R | title = Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli | journal = Journal of Bacteriology | volume = 178 | issue = 23 | pages = 6778–81 | date = December 1996 | pmid = 8955296 | pmc = 178575 | doi = 10.1128/jb.178.23.6778-6781.1996}}</ref> |
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The maximum specific enzymatic activity is 3.2 micromol/min/mg. The optimum pH is 7.5. The maximum pH is 8. The optimum temperature is 30 degrees Celsius and the maximum temperature is 40 degrees Celsius. The molecular weight of o-succinylbenzoate CoA ligase is 185000 Da or 185 kDa. This enzyme is a [[tetramer]], meaning it has four subunits in its [[Protein quaternary structure|quaternary structure]].<ref |
The maximum specific enzymatic activity is 3.2 micromol/min/mg. The optimum pH is 7.5. The maximum pH is 8. The optimum temperature is 30 degrees Celsius and the maximum temperature is 40 degrees Celsius. The molecular weight of o-succinylbenzoate CoA ligase is 185000 Da or 185 kDa. This enzyme is a [[tetramer]], meaning it has four subunits in its [[Protein quaternary structure|quaternary structure]].<ref name = "Kwon_1996" /> |
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The PDB accession code is [http://www.rcsb.org/pdb/explore/explore.do?job=summary&pdbId=3ipl 3ipl]. This is the crystal structure for o-succinylbenzoate CoA ligase in ''[[Staphylococcus aureus]]'' (strain N315) because the structure for ''[[E. coli]]'' has not been crystallized as of yet.<ref>{{Cite web|url = http://www.rcsb.org/pdb/explore/explore.do?structureId=3IPL|title = Crystal structure of o-succinylbenzoic acid-CoA ligase from Staphylococcus aureus|date |
The PDB accession code is [http://www.rcsb.org/pdb/explore/explore.do?job=summary&pdbId=3ipl 3ipl]. This is the crystal structure for o-succinylbenzoate CoA ligase in ''[[Staphylococcus aureus]]'' (strain N315) because the structure for ''[[E. coli]]'' has not been crystallized as of yet.<ref>{{Cite web|url = http://www.rcsb.org/pdb/explore/explore.do?structureId=3IPL|title = Crystal structure of o-succinylbenzoic acid-CoA ligase from Staphylococcus aureus|access-date = 6 December 2014|website = PDB|publisher = RCSB|last = Patskovsky, Toro, Dickey, Sauder, Chang, Burley, Almo}}</ref> |
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== Pathway == |
== Pathway == |
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The pathway o-succinylbenzoate CoA ligase belongs to is called 1, 4-dihydroxy-2-napthoate biosynthesis I. Other organisms that contain this pathway are eukaryotic bacteria such as ''[[Bacillus anthracis]]''.<ref>{{ |
The pathway o-succinylbenzoate CoA ligase belongs to is called 1, 4-dihydroxy-2-napthoate biosynthesis I. Other organisms that contain this pathway are eukaryotic bacteria such as ''[[Bacillus anthracis]]''.<ref>{{cite journal | vauthors = Tian Y, Suk DH, Cai F, Crich D, Mesecar AD | title = Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate | journal = Biochemistry | volume = 47 | issue = 47 | pages = 12434–47 | date = November 2008 | pmid = 18973344 | pmc = 2710618 | doi = 10.1021/bi801311d }}</ref> Organisms that contain a pathway similar to this include ''[[Arabidopsis thaliana]]'' (gene AAE14),<ref>{{cite journal | vauthors = Kim HU, van Oostende C, Basset GJ, Browse J | title = The AAE14 gene encodes the Arabidopsis o-succinylbenzoyl-CoA ligase that is essential for phylloquinone synthesis and photosystem-I function | journal = The Plant Journal | volume = 54 | issue = 2 | pages = 272–83 | date = April 2008 | pmid = 18208520 | doi = 10.1111/j.1365-313X.2008.03416.x | doi-access = free }}</ref> ''[[Mycobacterium phlei]]'',<ref>{{cite journal | vauthors = Sieweke HJ, Leistner E | title = o-Succinylbenzoate: coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis, displays broad specificity | journal = Zeitschrift für Naturforschung C | volume = 46 | issue = 7–8 | pages = 585–90 | date = August 1991 | pmid = 1663748 | doi = 10.1515/znc-1991-7-814| s2cid = 12789671 | doi-access = free }}</ref> ''' '''and ''[[Synechocystis|Synechocystis sp.]]'' (gene PCC 6803).<ref>{{Cite journal|title = The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803|last = Johnson, Naithani, Stewart Jr., Zybailov, Jones, Golbeck, Chitnis|date = 6 March 2003|journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics|doi = 10.1016/S0005-2728(02)00396-1|pmid =12615349|volume=1557|issue = 1–3|pages=67–76|doi-access = free}}</ref> The reason for the difference in pathways is due to the varying functions of Vitamin K. Eukaryotic bacteria use vitamin K II while other organisms use vitamin K I. Other pathways that include o-succinylbenzoate CoA ligase include 1, 4-diydroxy-2-naphthoate biosynthesis II (i.e. in Arabidopsis thaliana), biosynthesis of secondary metabolites, metabolic pathways, ubiquinone, and other terpenoid-quinone biosynthesis. In Bacillus anthracis this enzyme is a target of potential antibiotic discovery. |
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== Reaction == |
== Reaction == |
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ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA |
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA |
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The substrates of this reaction are [[Adenosine triphosphate|ATP]], [[Coenzyme A|CoA]], and [[2-succinylbenzoate]]. The cofactors are ATP and CoA. The products are [[Adenosine monophosphate|AMP]], [[diphosphate]], and [[4-(2-carboxyphenyl)-4-oxobutanoyl-CoA]].<ref>{{ |
The substrates of this reaction are [[Adenosine triphosphate|ATP]], [[Coenzyme A|CoA]], and [[2-succinylbenzoate]]. The cofactors are ATP and CoA. The products are [[Adenosine monophosphate|AMP]], [[diphosphate]], and [[4-(2-carboxyphenyl)-4-oxobutanoyl-CoA]].<ref>{{cite journal | vauthors = Kolkmann R, Leistner E | title = 4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis | journal = Zeitschrift für Naturforschung C | volume = 42 | issue = 11–12 | pages = 1207–14 | date = December 1987 | pmid = 2966501 | doi = 10.1515/znc-1987-11-1212| s2cid = 41701934 | doi-access = free }}</ref> |
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==References== |
== References == |
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{{Reflist}} |
{{Reflist}} |
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{{Ligases CO CS and CN}} |
{{Ligases CO CS and CN}} |
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{{Enzymes}} |
{{Enzymes}} |
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{{Portal bar|Biology|border=no}} |
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{{DEFAULTSORT:O-succinylbenzoate-CoA ligase}} |
{{DEFAULTSORT:O-succinylbenzoate-CoA ligase}} |
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Latest revision as of 15:13, 26 August 2023
| o-Succinylbenzoate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 A cartoon representation of O-succinylbenzoate Co-A ligase of Staphylococcus aureus (strain N315). The different subunits are shown in different colors. | |||||||||
| Identifiers | |||||||||
| EC no. | 6.2.1.26 | ||||||||
| CAS no. | 72506-70-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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o-Succinylbenzoate—CoA ligase (EC 6.2.1.26), encoded from the menE gene in Escherichia coli, catalyzes the fifth reaction in the synthesis of menaquinone (vitamin K2). This pathway is called 1, 4-dihydroxy-2-naphthoate biosynthesis I.[1] Vitamin K is a quinone that serves as an electron transporter during anaerobic respiration. This process of anaerobic respiration allows the bacteria to generate the energy required to survive.
Background
[edit]The systematic name for the MenE enzyme is 2-succinylbenzoate: CoA ligase (AMP-forming). Other names for this enzyme include: o-succinylbenzoate-CoA synthase; o-succinylbenzoyl-coenzyme A synthetase; OSB-CoA synthetase; OSB: CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. The EC number is 6.2.1.26. MenE belongs to the ligase enzyme family, or class 6.
In the presence of 0.5mM of Ca(2+), K(+), Na(+), and Zn(2+) the enzyme activity was increased twofold. In the presence of .5 mM of Co(2+) and Mn(2+) the enzyme activity was increased fourfold. Mg(2+) is the ion that increases the enzyme activity the most. With .5 mM of Mg(2+) enzyme activity was increased sixfold. Inhibitors of this enzyme include diethylprocarbonate, Fe(2+), Hg(2+), and Mg(2+) (above 1mM).[2]
The maximum specific enzymatic activity is 3.2 micromol/min/mg. The optimum pH is 7.5. The maximum pH is 8. The optimum temperature is 30 degrees Celsius and the maximum temperature is 40 degrees Celsius. The molecular weight of o-succinylbenzoate CoA ligase is 185000 Da or 185 kDa. This enzyme is a tetramer, meaning it has four subunits in its quaternary structure.[2]
The PDB accession code is 3ipl. This is the crystal structure for o-succinylbenzoate CoA ligase in Staphylococcus aureus (strain N315) because the structure for E. coli has not been crystallized as of yet.[3]
Pathway
[edit]The pathway o-succinylbenzoate CoA ligase belongs to is called 1, 4-dihydroxy-2-napthoate biosynthesis I. Other organisms that contain this pathway are eukaryotic bacteria such as Bacillus anthracis.[4] Organisms that contain a pathway similar to this include Arabidopsis thaliana (gene AAE14),[5] Mycobacterium phlei,[6] and Synechocystis sp. (gene PCC 6803).[7] The reason for the difference in pathways is due to the varying functions of Vitamin K. Eukaryotic bacteria use vitamin K II while other organisms use vitamin K I. Other pathways that include o-succinylbenzoate CoA ligase include 1, 4-diydroxy-2-naphthoate biosynthesis II (i.e. in Arabidopsis thaliana), biosynthesis of secondary metabolites, metabolic pathways, ubiquinone, and other terpenoid-quinone biosynthesis. In Bacillus anthracis this enzyme is a target of potential antibiotic discovery.
Reaction
[edit]The reaction in vitamin K synthesis that includes MenE is as follows:
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
The substrates of this reaction are ATP, CoA, and 2-succinylbenzoate. The cofactors are ATP and CoA. The products are AMP, diphosphate, and 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA.[8]
References
[edit]- ^ van Oostende, Widhalm, Furt, Ducluzeau, Basset (2011). Phylloquinone (Vitamin K1): function, enzymes and genes. Advances in Botanical Research: Academic Press (Amsterdam). pp. 229–61.
{{cite book}}: CS1 maint: multiple names: authors list (link) - ^ a b Kwon O, Bhattacharyya DK, Meganathan R (December 1996). "Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli". Journal of Bacteriology. 178 (23): 6778–81. doi:10.1128/jb.178.23.6778-6781.1996. PMC 178575. PMID 8955296.
- ^ Patskovsky, Toro, Dickey, Sauder, Chang, Burley, Almo. "Crystal structure of o-succinylbenzoic acid-CoA ligase from Staphylococcus aureus". PDB. RCSB. Retrieved 6 December 2014.
{{cite web}}: CS1 maint: multiple names: authors list (link) - ^ Tian Y, Suk DH, Cai F, Crich D, Mesecar AD (November 2008). "Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate". Biochemistry. 47 (47): 12434–47. doi:10.1021/bi801311d. PMC 2710618. PMID 18973344.
- ^ Kim HU, van Oostende C, Basset GJ, Browse J (April 2008). "The AAE14 gene encodes the Arabidopsis o-succinylbenzoyl-CoA ligase that is essential for phylloquinone synthesis and photosystem-I function". The Plant Journal. 54 (2): 272–83. doi:10.1111/j.1365-313X.2008.03416.x. PMID 18208520.
- ^ Sieweke HJ, Leistner E (August 1991). "o-Succinylbenzoate: coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis, displays broad specificity". Zeitschrift für Naturforschung C. 46 (7–8): 585–90. doi:10.1515/znc-1991-7-814. PMID 1663748. S2CID 12789671.
- ^ Johnson, Naithani, Stewart Jr., Zybailov, Jones, Golbeck, Chitnis (6 March 2003). "The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1557 (1–3): 67–76. doi:10.1016/S0005-2728(02)00396-1. PMID 12615349.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kolkmann R, Leistner E (December 1987). "4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis". Zeitschrift für Naturforschung C. 42 (11–12): 1207–14. doi:10.1515/znc-1987-11-1212. PMID 2966501. S2CID 41701934.
